AI Article Synopsis
- The study presents a novel design for a multi-domain cell-penetrating peptide amphiphile (CPPA) that can form fibrous structures and switch to spherical micelles when exposed to the enzyme MMP-2, which is found in tumor environments.
- This transformation allows the buried cell-penetrating peptide (CPP) to become exposed on the surface of the micelles, boosting their ability to penetrate cells.
- The CPP nanostructures are multifunctional and responsive to enzymes, making them promising candidates for targeted delivery of therapeutic and diagnostic agents directly to tumors.
Article Abstract
We report here a proof-of-concept design of a multi-domain cell-penetrating peptide amphiphile (CPPA) which can self-assemble into fibrous nanostructures and transform into spherical micelles upon enzymatic degradation by matrix metalloproteinase-2 (MMP-2) up-regulated in the tumour environment. Concomitant with this morphological transition, the cell-penetrating peptide (CPP), which was previously buried inside the CPPA fibers, could be presented on the surface of the CPPA micelles, enhancing their cell-penetrating ability. These multifunctional and enzyme-responsive CPP nanostructures hold potential as nanocarriers for tumour-targeted intracellular delivery of therapeutic and diagnostic agents.
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| http://dx.doi.org/10.1039/c7cc03512h | DOI Listing |
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